Professor Mostafa El-Sayed Wins 2016 Priestley Medal

The American Chemical Society, the world’s largest scientific society, has announced Georgia Tech Professor Mostafa El-Sayed as the winner of its highest honor, the 2016 Priestley Medal for distinguished service in the field of Chemistry.

Summer First Fellows on the ropes

Our 2015 Summer First Fellows, drawn from graduate students admitted to Chemistry, Physics and Bioinformatics, started their time at GT with a morning on the leadership challenge course along with current students, faculty and staff.

2015 REU Program Commences with Annual Retreat

Welcome to the 2015 REU students who arrived on campus this week to participate in the 10 week program.

Bonjour….Chemistry in Lyon, France 2015

Thirty-six Georgia Tech undergraduates are currently participating in an 8-week GT faculty-led study abroad program in Lyon, France.

Seminars & Events

Meeting - Thursday, July 16, 2015 - 11:00am - MoSE 2100F
Meeting - Tuesday, July 21, 2015 - 11:00am - MoSE 3201A
Meeting - Thursday, August 13, 2015 - 11:00am - MoSE 2100F
Meeting - Tuesday, August 18, 2015 - 11:00am - MoSE 3201A

Featured Research

Article Title
Research Authors
Johanna M. Smeekens, Weixuan Chen, Ronghu Wu .
Journal of the American Society for Mass Spectrometry (2015), Vol. 26(4), 604-614
Miscellaneous Details
This work was supported by start-up funds from Georgia Institute of Technology. R.W. is also supported by the Blanchard Assistant Professorship.

Cell surface N-glycoproteins play extraordinarily important roles in cell-cell communication, cell-matrix interactions, and cellular response to environmental cues. Global analysis is exceptionally challenging because many N-glycoproteins are present at low abundances and   effective separation is difficult to achieve. Here, we have developed a novel strategy integrating metabolic labeling, copper-free click chemistry, and mass spectrometry (MS)-based proteomics methods to analyze cell surface N-glycoproteins comprehensively and site-specifically. A sugar analog containing an azido group, N-azidoacetylgalactosamine, was fed to cells to label glycoproteins. Glycoproteins with the functional group on the cell surface were then bound to dibenzocyclooctyne-sulfo-biotin via copper-free click chemistry under physiological conditions. After protein extraction and digestion, glycopeptides with the biotin tag were enriched by NeutrAvidin conjugated beads. Enriched glycopeptides were deglycosylated with peptide-N-glycosidase F in heavy-oxygen water, and in the process of glycan removal, asparagine was converted to aspartic acid and tagged with 18O for MS analysis. With this strategy, 144 unique N-glycopeptides containing 152 N-glycosylation sites were identified in 110 proteins in HEK293T cells. As expected, 95% of identified glycoproteins were membrane proteins, which were highly enriched. Many sites were located on important receptors, transporters, and cluster of differentiation proteins. The experimental results demonstrated that the current method is very effective for the comprehensive and site-specific identification of the cell surface N-glycoproteome and can be
extensively applied to other cell surface protein studies.

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